Hydrophobic scale: a second parameter to elucidating various specific ligand-protein interactions.

Naganori Numao; Hisashi Fujii; Yoshiyuki Fukazawa; Nobutaka Hanagata; Kazuyoshi Tanaka

doi:10.1248/cpb.52.377

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Hydrophobic scale: a second parameter to elucidating various specific ligand-protein interactions.

Naganori Numao·Hisashi Fujii·Yoshiyuki Fukazawa·Nobutaka Hanagata·Kazuyoshi Tanaka

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Abstract

In the sequence Fourier analysis (SFA) of specific interactions such as those between fibroblast growth factors (FGFs)/FGF receptors (FGFRs), bone morphogenetic proteins (BMPs)/BMP receptors (BMPRs), or tumor repressor protein p53/mouse double minute 2 homolog (MDM2), the characteristic frequency peak(s) could be observed with the hydrophobic scale for 20 amino acids as well as 4 nucleotides as the physicochemical parameter, but not successfully with the absolute electronegativity scale. This result implies that these two independent scales should be appropriately selected in various specific ligand-protein interactions, though the critical difference has to be determined.

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Amino Acid Sequence Animals Bone Morphogenetic Proteins Drosophila Escherichia coli Fibroblast Growth Factors Fourier Analysis Humans Ligands Mice Models, Molecular Nucleotides Oryza Proteins Saccharomyces cerevisiae Sequence Analysis Tumor Suppressor Protein p53 Journal Article

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Naganori Numao, Hisashi Fujii, Yoshiyuki Fukazawa, Nobutaka Hanagata, Kazuyoshi Tanaka. 2004. Hydrophobic scale: a second parameter to elucidating various specific ligand-protein interactions.. https://doi.org/10.1248/cpb.52.377

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